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6RNR

The crystal structure of a complex between the LlFpg protein, a THF-DNA and an inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0003677molecular_functionDNA binding
A0003684molecular_functiondamaged DNA binding
A0003906molecular_functionDNA-(apurinic or apyrimidinic site) endonuclease activity
A0006281biological_processDNA repair
A0006284biological_processbase-excision repair
A0008270molecular_functionzinc ion binding
A0008534molecular_functionoxidized purine nucleobase lesion DNA N-glycosylase activity
A0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
A0019104molecular_functionDNA N-glycosylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue KBN A 301
ChainResidue
ALYS57
ALEU161
AARG260
DDT8
DDT9
DDT10

site_idAC2
Number of Residues9
Detailsbinding site for residue GOL A 302
ChainResidue
ATHR113
AGLU115
ATYR125
ALYS129
DDT9
DDT10
ATYR58
AHIS72
AARG74

Functional Information from PROSITE/UniProt
site_idPS01242
Number of Residues25
DetailsZF_FPG_1 Zinc finger FPG-type signature. Csr..CGaeIqkikvag....RGthFCpvCQ
ChainResidueDetails
ACYS245-GLN269

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues34
DetailsZN_FING: FPG-type
ChainResidueDetails
AGLN236-GLN270

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Schiff-base intermediate with DNA => ECO:0000305
ChainResidueDetails
APRO1

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305
ChainResidueDetails
AGLU2

site_idSWS_FT_FI4
Number of Residues1
DetailsACT_SITE: Proton donor; for beta-elimination activity => ECO:0000305
ChainResidueDetails
ALYS57

site_idSWS_FT_FI5
Number of Residues1
DetailsACT_SITE: Proton donor; for delta-elimination activity => ECO:0000305
ChainResidueDetails
AARG260

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AHIS91
AARG109

221051

PDB entries from 2024-06-12

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